Nature子刊：于杰团队等揭示人源牛磺酸转运蛋白TauT的二聚化和底物识别机制

Core Viewpoint - The article discusses the significance of taurine and its transporter TauT, highlighting recent research that reveals the structural and functional mechanisms of TauT, which may have implications for understanding taurine-related diseases and potential therapeutic strategies [2][9]. Group 1: Taurine and TauT Overview - Taurine is a sulfur-containing β-amino acid essential for various physiological functions, including cell stability, neurotransmission regulation, lipid metabolism, and antioxidant activity [2]. - The ability to synthesize taurine decreases with age, making external intake via TauT crucial [2]. Group 2: Recent Research Findings - A study published in Nature Communications by the Shanghai Institute of Organic Chemistry identified multiple oligomeric states of human TauT in a nanodisc environment using cryo-electron microscopy [3]. - The research revealed a novel dimerization mechanism for TauT, differing from other transporters in the SLC6 family, with cholesterol playing a role in facilitating this oligomerization [6]. Group 3: Mechanism of Substrate Recognition and Transport - The study detailed the structural dynamics of TauT in various states, elucidating its substrate specificity and transport mechanism, where the central site can bind one substrate, two Na⁺, and one Cl⁻, transitioning from an open to a closed state [7]. - Key residues Gly57 and Phe58 are critical for substrate specificity, undergoing conformational changes during substrate release [7][12]. Group 4: Implications for Health and Disease - The findings underscore the importance of lipid microenvironments in regulating TauT oligomerization and provide a structural framework for understanding TauT's function, which may aid in exploring treatment strategies for diseases related to taurine deficiency [9].